Evidence map›Paper›PMID 19212143›Full record

ReviewNeuro-Signals2009

Heterotrimeric G-proteins interact directly with cytoskeletal components to modify microtubule-dependent cellular processes.

Rahul H Dave, Witchuda Saengsawang, Jiang-Zhou Yu, Robert Donati, Mark M Rasenick

Open access · bronzeAbstract readReview
In one paragraph

Review in Neuro-Signals, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.1field-weighted citation impact, top 14% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

17 citing papers in PubMed, 44 citations in OpenAlex.

  1. The Role and Mechanisms of G protein-coupled receptors in Parkinson's disease.Neurological sciences : official journal of the Italian Neurological Society and of the Italian Society of Clinical Neurophysiology · 2025
    Review
  2. Review
  3. Review
  4. Disruption of lipid-raft localized GαNeuropsychopharmacology : official publication of the American College of Neuropsychopharmacology · 2018
    Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. Arborization of dendrites by developing neocortical neurons is dependent on primary cilia and type 3 adenylyl cyclase.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2013
    Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 3 institutions in 2 countries.

Rahul H DaveDepartment of Physiology and Biophysics, University of Illinois Chicago, Chicago, Il 60612-7342, USA.
Witchuda Saengsawang
Jiang-Zhou Yu
Robert Donati
Mark M Rasenick
Institute of Molecular Biology and Biophysics · RUIllinois College of Optometry · USUniversity of Illinois Chicago · US

Funding

TRAINING IN CELLULAR SIGNALLING IN THE CARDIOVASCULAR SYT32HL007692 · NHLBI · UNIVERSITY OF ILLINOIS AT CHICAGO · PI SOLARO, R JOHN · 1990 to 2014
$8.5M
CYTOSKELETAL INTERACTION WITH NEURONAL ADENYLATE CYCLASER01MH039595 · NIMH · UNIVERSITY OF ILLINOIS AT CHICAGO · PI RASENICK, MARK M · 1985 to 2006
$2.0M
Post-Synaptic Mechanisms for Depression and Antidepressants: Studies in Model SyR01MH078200 · NIMH · UNIVERSITY OF ILLINOIS AT CHICAGO · PI RASENICK, MARK M. · 2008 to 2010
$519k
Structural basis for reciprocal regulation of the GTPases tubulin and GsalphaR21DA020568 · NIDA · UNIVERSITY OF ILLINOIS AT CHICAGO · PI RASENICK, MARK M · 2005 to 2006
$314k
NHLBI NIH HHS T32 HL007692NHLBI NIH HHS T32 HL-07692NIDA NIH HHS DA 20568NIDA NIH HHS R21 DA020568NIMH NIH HHS MH 39595NIMH NIH HHS MH78200NIMH NIH HHS R01 MH039595NIMH NIH HHS R01 MH078200
6 · The paper itself

Abstract

A large percentage of current drugs target G-protein-coupled receptors, which couple to well-known signaling pathways involving cAMP or calcium. G-proteins themselves may subserve a second messenger function. Here, we review the role of tubulin and microtubules in directly mediating effects of heterotrimeric G-proteins on neuronal outgrowth, shape and differentiation. G-protein-tubulin interactions appear to be regulated by neurotransmitter activity, and, in turn, regulate the location of Galpha in membrane microdomains (such as lipid rafts) or the cytosol. Tubulin binds with nanomolar affinity to Gsalpha, Gialpha1 and Gqalpha (but not other Galpha subunits) as well as Gbeta(1)gamma(2) subunits. Galpha subunits destabilize microtubules by stimulating tubulin's GTPase, while Gbetagamma subunits promote microtubule stability. The same region on Gsalpha that binds adenylyl cyclase and Gbetagamma also interacts with tubulin, suggesting that cytoskeletal proteins are novel Galpha effectors. Additionally, intracellular Gialpha-GDP, in concert with other GTPase proteins and Gbetagamma, regulates the position of the mitotic spindle in mitosis. Thus, G-protein activation modulates cell growth and differentiation by directly altering microtubule stability. Further studies are needed to fully establish a structural mechanism of this interaction and its role in synaptic plasticity.

Indexed as

Adenylyl CyclasesAnimalsCell MembraneCytosolGTP PhosphohydrolasesHeterotrimeric GTP-Binding ProteinsHumansMicrotubulesModels, MolecularNeurogenesisNeuronsNeurotransmitter AgentsProtein StabilityProtein Structure, QuaternarySpindle ApparatusTubulinAdenylyl CyclasesGTP PhosphohydrolasesHeterotrimeric GTP-Binding ProteinsNeurotransmitter AgentsTubulin

Identifiers

PMID19212143
PMCPMC2836952
OpenAlexW2039328925

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.